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. 2022 Jan 27;7(5):3836–3843. doi: 10.1021/acsomega.1c04726

Figure 1.

Figure 1

UPS and deubiquitinating enzymes. (1) Ubiquitin (Ub)-activating E1 enzyme transfers ubiquitin to the ubiquitin-conjugating E2 enzyme, which, together with ubiquitin E3 ligase, transfers Ub to the target protein, forming the polyubiquitinated substrate. (2) 19S Ub receptors (Rpn1, Rpn10, and Rpn13) recognize PS deubiquitinating enzymes (Rpn11, UCHL5, and USP14 deubiquitinate PS) and degrade it inside 20S, and the β1, β2, and β5 subunits perform the catalysis (blue). (3) Polyubiquitin chain is cleaved by the deubiquinating enzymes (DUBs), which keep the Ub pool inside the cell. Six ATPase subunits (Rpt1–Rpt6) and non-ATPase subunits are in purple and red, respectively.